EGFR Protein, Mouse (Biotinylated, HEK293, His-Avi)

EGFR Protein, a receptor tyrosine kinase, binds ligands of the EGF family, such as EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG, and HBEGF/heparin-binding EGF, activating multiple signaling cascades to transduce extracellular cues into cellular responses. Ligand binding induces receptor homo- and/or heterodimerization, leading to autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2, initiating downstream signaling cascades, including RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC, and STATs modules. EGFR may also activate the NF-kappa-B signaling cascade and directly phosphorylate proteins like RGS16, modulating G protein-coupled receptor signaling. Additionally, EGFR phosphorylates MUC1, enhancing its interaction with SRC and CTNNB1/beta-catenin. Notably, it positively regulates cell migration through interaction with CCDC88A/GIV, promoting EGFR signaling and triggering cell migration. EGFR also plays a role in enhancing learning and memory performance and contributes to mammalian pain signaling, leading to long-lasting hypersensitivity.